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Q9U8B8

- DYR_HELVI

UniProt

Q9U8B8 - DYR_HELVI

Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Heliothis virescens (Tobacco budworm moth)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis By similarity.By similarity

    Catalytic activityi

    5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.By similarityPROSITE-ProRule annotation

    Enzyme regulationi

    Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei71 – 711SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 237NADPBy similarity
    Nucleotide bindingi55 – 573NADPBy similarity
    Nucleotide bindingi77 – 793NADPBy similarity
    Nucleotide bindingi117 – 1248NADPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: UniProtKB-EC
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. glycine biosynthetic process Source: InterPro
    2. nucleotide biosynthetic process Source: InterPro
    3. one-carbon metabolic process Source: UniProtKB-KW
    4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrofolate reductase (EC:1.5.1.3)
    Gene namesi
    Name:DHFR
    OrganismiHeliothis virescens (Tobacco budworm moth)Imported
    Taxonomic identifieri7102 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHeliothis

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Dihydrofolate reductasePRO_0000186371Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ9U8B8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 184180DHFRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni31 – 366Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the dihydrofolate reductase family.Curated
    Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.430.10. 1 hit.
    InterProiIPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view]
    PfamiPF00186. DHFR_1. 1 hit.
    [Graphical view]
    PRINTSiPR00070. DHFR.
    SUPFAMiSSF53597. SSF53597. 1 hit.
    PROSITEiPS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9U8B8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA    50
    VIMGRRTWDC IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA 100
    IKYIEGREDI ESTWVIGGSS IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP 150
    NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR VYKKL 185
    Length:185
    Mass (Da):21,089
    Last modified:May 1, 2000 - v1
    Checksum:i9B8C0E50ED175812
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51K → L AA sequence (PubMed:10632709)Curated
    Sequence conflicti7 – 71N → D AA sequence (PubMed:10632709)Curated
    Sequence conflicti11 – 133AAC → IFD AA sequence (PubMed:10632709)Curated
    Sequence conflicti15 – 151N → D AA sequence (PubMed:10632709)Curated
    Sequence conflicti21 – 211N → D AA sequence (PubMed:10632709)Curated
    Sequence conflicti158 – 1581H → Q AA sequence (PubMed:10632709)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104106 mRNA. Translation: AAF04459.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF104106 mRNA. Translation: AAF04459.1 .

    3D structure databases

    ProteinModelPortali Q9U8B8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .

    Family and domain databases

    Gene3Di 3.40.430.10. 1 hit.
    InterProi IPR012259. DHFR.
    IPR024072. DHFR-like_dom.
    IPR017925. DHFR_CS.
    IPR001796. DHFR_dom.
    [Graphical view ]
    Pfami PF00186. DHFR_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00070. DHFR.
    SUPFAMi SSF53597. SSF53597. 1 hit.
    PROSITEi PS00075. DHFR_1. 1 hit.
    PS51330. DHFR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tobacco budworm dihydrofolate reductase is a promising target for insecticide discovery."
      Walker V.K., Tyshenko M.G., Kuiper M.J., Dargar R.V., Yuhas D.A., Cruickshank P.A., Chaguturu R.
      Eur. J. Biochem. 267:394-403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 3-22; 32-38; 143-149; 153-159 AND 170-175, ENZYME REGULATION.
      Tissue: Larva.

    Entry informationi

    Entry nameiDYR_HELVI
    AccessioniPrimary (citable) accession number: Q9U8B8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3